Structure of HLA-A*1101 in complex with a hepatitis B peptide homologue
Research output: Contribution to journal › Journal article › peer-review
A high-resolution structure of the human MHC-I molecule HLA-A*1101 is presented in which it forms a complex with a sequence homologue of a peptide that occurs naturally in hepatitis B virus DNA polymerase. The sequence of the bound peptide is AIMPARFYPK, while that of the corresponding natural peptide is LIMPARFYPK. The peptide does not make efficient use of the middle E pocket for binding, which leads to a rather superficial and exposed binding mode for the central peptide residues. Despite this, the peptide binds with high affinity (IC50 of 31 nM).
Original language | English |
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Journal | Acta Crystallographica Section F-Structural Biology and Crystallization Communications |
Volume | 62 |
Issue number | Pt 12 |
Pages (from-to) | 1179-84 |
Number of pages | 5 |
DOIs | |
Publication status | Published - 2006 |
Bibliographical note
Keywords: Amino Acid Sequence; Crystallization; DNA-Directed DNA Polymerase; HLA-A Antigens; Hepatitis B virus; Humans; Hydrogen Bonding; Oligopeptides; Peptide Fragments; Protein Binding; Protein Conformation
ID: 9942600